BaH4 hemorrhagic metalloproteinase, Bothrops asper

Known as: BaH4 protein, Bothrops asper 
 
National Institutes of Health

Topic mentions per year

Topic mentions per year

1986-2013
01219862013

Papers overview

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2013
2013
Bothrops snakes are the major cause of ophidian envenomings in Latin America. Their venom contains myotoxins that cause prominent… (More)
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2012
2012
Lys49-PLA2 myotoxins, an important component of various viperid snake venoms, are a class of PLA2-homolog proteins deprived of… (More)
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2011
2011
Lys49 phospholipase A2 (PLA2) homologues present in crotalid snake venoms lack enzymatic activity, yet they induce skeletal… (More)
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Review
2009
Review
2009
Inflammation is a major characteristic of envenomation by snakes from viperine and crotaline species. Bothrops asper snake venom… (More)
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1987
1987
The binding of Bothrops asper myotoxin to mouse skeletal muscle was studied at both the light and electron microscope levels… (More)
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1987
1987
Metalloproteinase from the venom of Bothrops asper (proteinase G) is a glycoprotein with 1% neutral hexose and 3.5 moles of… (More)
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1986
1986
In order to assess the extent of regeneration, creatine kinase content of injected gastrocnemius muscle were determined at four… (More)
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